ArticleThe EMBO journal1996
Binding and kinetic properties of HIV-1 reverse transcriptase markedly differ during initiation and elongation of reverse transcription.
Article in The EMBO journal, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
56 citing papers in PubMed.
- May I Help You with Your Coat? HIV-1 Capsid Uncoating and Reverse Transcription.International journal of molecular sciences · 2024Review
- Retroviral PBS-segment sequence and structure: Orchestrating early and late replication events.Retrovirology · 2024Review
- Internal RNA 2'-O-methylation on the HIV-1 genome impairs reverse transcription.Nucleic acids research · 2024Article
- Review
- Insights into HIV-1 Reverse Transcriptase (RT) Inhibition and Drug Resistance from Thirty Years of Structural Studies.Viruses · 2022Review
- High-resolution view of HIV-1 reverse transcriptase initiation complexes and inhibition by NNRTI drugs.Nature communications · 2021Article
- Advances in understanding the initiation of HIV-1 reverse transcription.Current opinion in structural biology · 2020Review
- Distinct Conformational States Underlie Pausing during Initiation of HIV-1 Reverse Transcription.Journal of molecular biology · 2020Article
- DNA polymerase activity on synthetic N3'→P5' phosphoramidate DNA templates.Nucleic acids research · 2019Article
- Virion-associated, host-derived DHX9/RNA helicase A enhances the processivity of HIV-1 reverse transcriptase on genomic RNA.The Journal of biological chemistry · 2019Article
- Relating Structure and Dynamics in RNA Biology.Cold Spring Harbor perspectives in biology · 2019Review
- Structure of HIV-1 RT/dsRNA initiation complex prior to nucleotide incorporation.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Illuminating the virus life cycle with single-molecule FRET imaging.Advances in virus research · 2019Article
- Dynamic Interplay of RNA and Protein in the Human Immunodeficiency Virus-1 Reverse Transcription Initiation Complex.Journal of molecular biology · 2018Article
- Effect of tRNA on the Maturation of HIV-1 Reverse Transcriptase.Journal of molecular biology · 2018Article
- Article
- HIV-1 Integrates Widely throughout the Genome of the Human Blood Fluke Schistosoma mansoni.PLoS pathogens · 2016Article
- Genetic encoding of DNA nanostructures and their self-assembly in living bacteria.Nature communications · 2016Article
- Interaction between Reverse Transcriptase and Integrase Is Required for Reverse Transcription during HIV-1 Replication.Journal of virology · 2015Article
- A mutant tat protein inhibits HIV-1 reverse transcription by targeting the reverse transcription complex.Journal of virology · 2015Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
We recently showed that primer tRNA3Lys, human immunodeficiency virus type 1 (HIV-1) RNA and HIV-1 reverse transcriptase (RT) form a specific complex of initiation of reverse transcription that can be functionally distinguished from the elongation complex, which can be obtained by substituting an 18mer oligodeoxyribonucleotide (ODN) for the natural primer (Isel et al., 1996). Here, we compared the binding properties and the single and multiple turnover kinetics of HIV-1 RT in the initiation and elongation complexes. Even though the equilibrium dissociation constants of HIV-1 RT are not very different for the two complexes, RT dissociates approximately 200-fold faster from the initiation complex. Furthermore, nucleotide incorporation by the pre-formed primer-template-RT complexes is reduced by a approximately 50-fold factor during initiation of reverse transcription, compared with elongation. As a consequence, processivity of HIV-1 RT in the initiation complex is close to unity, while it increases by four orders of magnitude during elongation, as expected for a replication enzyme. This processivity change is reminiscent of the transition from initiation to elongation of transcription. Furthermore, our results indicate that the post-transcriptional modifications of tRNA3Lys play a role similar to that of the sigma factor in transcription by the Escherichia coli RNA polymerase: they favour the formation of the specific initiation complex but do not affect the polymerization rate of the bound enzyme.
Indexed as
Identifiers
9003793PMC452545What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.